STI1/YOR027W Literature Guide Help

Other names published for STI1: YOR027W

STI1 - Function/Process (27)

ReferenceOther Genes Addressed
Li J, et al.  (2011) Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle. Nat Struct Mol Biol 18(1):61-6
Rossignol T, et al.  (2009) The proteome of a wine yeast strain during fermentation, correlation with the transcriptome. J Appl Microbiol 107(1):47-55
Fan Q, et al.  (2007) The Role of Sse1 in the de Novo Formation and Variant Determination of the [PSI+] Prion. Genetics 177(3):1583-93
Flom G, et al.  (2006) Effect of mutation of the tetratricopeptide repeat and asparatate-proline 2 domains of Sti1 on Hsp90 signaling and interaction in Saccharomyces cerevisiae. Genetics 172(1):41-51
Wegele H, et al.  (2006) Substrate transfer from the chaperone Hsp70 to Hsp90. J Mol Biol 356(3):802-11
Flom G, et al.  (2005) Novel interaction of the Hsp90 chaperone machine with Ssl2, an essential DNA helicase in Saccharomyces cerevisiae. Curr Genet 47(6):368-80
Jones G, et al.  (2004) Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding. Mol Cell Biol 24(9):3928-37
Lee P, et al.  (2004) Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase. Mol Biol Cell 15(4):1785-92
Nelson GM, et al.  (2004) The heat shock protein 70 cochaperone hip enhances functional maturation of glucocorticoid receptor. Mol Endocrinol 18(7):1620-30
Piper PW, et al.  (2003) Sensitivity to Hsp90-targeting drugs can arise with mutation to the Hsp90 chaperone, cochaperones and plasma membrane ATP binding cassette transporters of yeast. Eur J Biochem 270(23):4689-95
Richter K, et al.  (2003) Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle. J Biol Chem 278(12):10328-33
Wegele H, et al.  (2003) Sti1 is a novel activator of the Ssa proteins. J Biol Chem 278(28):25970-6
Abbas-Terki T, et al.  (2002) The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically. Biol Chem 383(9):1335-42
Kryndushkin DS, et al.  (2002) Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions. J Biol Chem 277(26):23702-8
Lee P, et al.  (2002) The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability. J Cell Biol 159(6):1051-9
Abbas-Terki T, et al.  (2001) Hsp104 interacts with Hsp90 cochaperones in respiring yeast. Mol Cell Biol 21(22):7569-75
Donze O and Picard D  (1999) Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2 [corrected]. Mol Cell Biol 19(12):8422-32
Jones MH, et al.  (1999) Yeast Dam1p is required to maintain spindle integrity during mitosis and interacts with the Mps1p kinase. Mol Biol Cell 10(7):2377-91
Liu XD, et al.  (1999) The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone. J Biol Chem 274(38):26654-60
Nathan DF, et al.  (1999) Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. Proc Natl Acad Sci U S A 96(4):1409-14
Prodromou C, et al.  (1999) Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)-domain co-chaperones. EMBO J 18(3):754-62
Baxter BK and Craig EA  (1998) Suppression of an Hsp70 mutant phenotype in Saccharomyces cerevisiae through loss of function of the chromatin component Sin1p/Spt2p. J Bacteriol 180(24):6484-92
Delling U, et al.  (1998) Identification of Saccharomyces cerevisiae genes conferring resistance to quinoline ring-containing antimalarial drugs. Antimicrob Agents Chemother 42(5):1034-41
Fang Y, et al.  (1998) SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins. Mol Cell Biol 18(7):3727-34
Johnson BD, et al.  (1998) Hop modulates Hsp70/Hsp90 interactions in protein folding. J Biol Chem 273(6):3679-86
Chang HC, et al.  (1997) In vivo analysis of the Hsp90 cochaperone Sti1 (p60). Mol Cell Biol 17(1):318-25
Nicolet CM and Craig EA  (1989) Isolation and characterization of STI1, a stress-inducible gene from Saccharomyces cerevisiae. Mol Cell Biol 9(9):3638-46